1fdp

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[[Image:1fdp.gif|left|200px]]
 
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{{Structure
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==PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D==
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|PDB= 1fdp |SIZE=350|CAPTION= <scene name='initialview01'>1fdp</scene>, resolution 2.1&Aring;
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<StructureSection load='1fdp' size='340' side='right'caption='[[1fdp]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE= <scene name='pdbsite=TRA:Catalytic+Triad'>TRA</scene>, <scene name='pdbsite=TRB:Catalytic+Triad'>TRB</scene>, <scene name='pdbsite=TRC:Catalytic+Triad'>TRC</scene> and <scene name='pdbsite=TRD:Catalytic+Triad'>TRD</scene>
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1fdp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FDP FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Complement_factor_D Complement factor D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.46 3.4.21.46] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdp OCA], [https://pdbe.org/1fdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fdp RCSB], [https://www.ebi.ac.uk/pdbsum/1fdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdp ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Disease ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdp OCA], [http://www.ebi.ac.uk/pdbsum/1fdp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fdp RCSB]</span>
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[https://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:[https://omim.org/entry/613912 613912]. CFDD is an immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway.
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}}
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== Function ==
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[https://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN] Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/1fdp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fdp ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of profactor D, determined at 2.1 A resolution with an Rfree and an R-factor of 25.1 and 20.4%, respectively, displays highly flexible or disordered conformation for five regions: N-22, 71-76, 143-152, 187-193 and 215-223. A comparison with the structure of its mature serine protease, complement factor D, revealed major conformational changes in the similar regions. Comparisons with the zymogen-active enzyme pairs of chymotrypsinogen, trypsinogen and prethrombin-2 showed a similar distribution of the flexible regions. However, profactor D is the most flexible of the four, and its mature enzyme displays inactive, self-inhibited active site conformation. Examination of the surface properties of the N-terminus-binding pocket indicates that Ile16 may play the initial positioning role for the N-terminus, and Leu17 probably also helps in inducing the required conformational changes. This process, perhaps shared by most chymotrypsinogen-like zymogens, is followed by a factor D-unique step, the re-orientation of an external Arg218 to an internal position for salt-bridging with Asp189, leading to the generation of the self-inhibited factor D.
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'''PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D'''
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Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D.,Jing H, Macon KJ, Moore D, DeLucas LJ, Volanakis JE, Narayana SV EMBO J. 1999 Feb 15;18(4):804-14. PMID:10022823<ref>PMID:10022823</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1fdp" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The crystal structure of profactor D, determined at 2.1 A resolution with an Rfree and an R-factor of 25.1 and 20.4%, respectively, displays highly flexible or disordered conformation for five regions: N-22, 71-76, 143-152, 187-193 and 215-223. A comparison with the structure of its mature serine protease, complement factor D, revealed major conformational changes in the similar regions. Comparisons with the zymogen-active enzyme pairs of chymotrypsinogen, trypsinogen and prethrombin-2 showed a similar distribution of the flexible regions. However, profactor D is the most flexible of the four, and its mature enzyme displays inactive, self-inhibited active site conformation. Examination of the surface properties of the N-terminus-binding pocket indicates that Ile16 may play the initial positioning role for the N-terminus, and Leu17 probably also helps in inducing the required conformational changes. This process, perhaps shared by most chymotrypsinogen-like zymogens, is followed by a factor D-unique step, the re-orientation of an external Arg218 to an internal position for salt-bridging with Asp189, leading to the generation of the self-inhibited factor D.
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*[[Complement factor 3D structures|Complement factor 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1FDP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDP OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D., Jing H, Macon KJ, Moore D, DeLucas LJ, Volanakis JE, Narayana SV, EMBO J. 1999 Feb 15;18(4):804-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10022823 10022823]
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[[Category: Complement factor D]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Delucas, L J.]]
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[[Category: Delucas LJ]]
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[[Category: Jing, H.]]
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[[Category: Jing H]]
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[[Category: Macon, K J.]]
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[[Category: Macon KJ]]
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[[Category: Moore, D.]]
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[[Category: Moore D]]
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[[Category: Narayana, S V.L.]]
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[[Category: Narayana SVL]]
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[[Category: Volanakis, J E.]]
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[[Category: Volanakis JE]]
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[[Category: complement]]
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[[Category: factor d]]
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[[Category: proenzyme]]
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[[Category: profactor d]]
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[[Category: serine protease]]
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[[Category: zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:20:54 2008''
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Current revision

PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D

PDB ID 1fdp

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